A series of new chiral phosphine-phosphoramidite ligands with a 3,3'-substituted binaphthyl moiety were prepared from 1-phenylethylamine, and successfully applied in the Rh-catalyzed asymmetric hydrogenation of beta-(acylamino)-acrylates. The research disclosed that the substituents on the 3,3'-positions of binaphthyl moiety significantly influenced the enantioselectivity.

Highly Enantioselective Rh-Catalyzed Hydrogenation of β-(Acylamino)acrylates: Significant Effect of Substituents on 3,3'-Positions of Binaphthyl Moiety. -Introduction of phenyl substituents at the phosphoramidite backbone of PEAPhos ligand (PEAPP) significantly increases its catalytic activity in the Rh-catalyzed asymmetric hydrogenation of β-(acylamino)acrylates. β-Aryl-β-aminocarboxylates (II) are formed in up to >99% optical purity. -(ZHOU, X.-M.; HUANG, J.-D.; LUO, L.-B.; ZHANG, C.-L.; HU*, X.-P.; ZHENG, Z.; Org.

The development of novel methods for highly efficient protein purification remains a research focus in the biotechnology field because conventional purification approaches, including affinity purification, gel filtration, and ionexchange chromatography, require complex manipulation steps and are costly. Here, we describe a simple and rapid protein purification strategy in which the SUMO tag and Ulp1 protease are surface-displayed separately on Escherichia coli cells. After protein induction, the cells are harvested, resuspended in cleavage buffer, and incubated together for cleavage. In this approach, the surface-displayed Ulp1 cleaves the membrane-anchored SUMO fusion protein, resulting in the release of the target protein from the C-terminal of SUMO into the solution. The bacterial cells harboring SUMO and Ulp1 on their surfaces can be easily removed by centrifugation. To evaluate the purification method, we used red fluorescent protein (mCherry). Purified mCherry protein (7.72 ± 1.05 mg from 1 L of bacterial culture) was obtained after only 30 min of incubation. The protein purity was higher than 80%, and could be further improved (> 90%) by simple ultrafiltration. This study offers a promising and simple strategy for the purification of recombinant protein in its native form that requires only cleavage and centrifugation steps.